The roles of two O-donor ligands in the Fe2+-binding and H2O2-sensing by the Fe2+-dependent H2O2 sensor PerR
DC Field | Value | Language |
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dc.contributor.author | Ji, Chang-Jun | - |
dc.contributor.author | Yang, Yoon Mo | - |
dc.contributor.author | Kim, Jung-Hoon | - |
dc.contributor.author | Ryu, Su-Hyun | - |
dc.contributor.author | Youn, Hwan | - |
dc.contributor.author | Lee, Jin-Won | - |
dc.date.accessioned | 2021-08-02T13:29:10Z | - |
dc.date.available | 2021-08-02T13:29:10Z | - |
dc.date.created | 2021-05-12 | - |
dc.date.issued | 2018-06 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/16913 | - |
dc.description.abstract | PerR is a metal-dependent peroxide sensing transcription factor which controls the expression of genes involved in peroxide resistance. The function of Bacillus subtilis PerR is mainly dictated by the regulatory metal ion (Fe2+ or Mn2+) coordinated by three N-donor ligands (His37, His91, and His93) and two 0 donor ligands (Asp85 and Asp104). While H2O2 sensing by PerR is mediated by Fe2+-dependent oxidation of N-donor ligand (either His37 or His91), one of the O-donor ligands (Asp104), but not Asp85, has been proposed as the key residue that regulates the sensitivity of PerR to H2O2. Here we systematically investigated the relative roles of two O-donor ligands of PerR in metal-binding affinity and H2O2 sensitivity in vivo and in vitro. Consistent with the previous report, in vitro the D104E-PerR could not sense low levels of H2O2 in the presence of excess Fe2+ sufficient for the formation of the Fe2+-bound D104E-PerR. However, the expression of PerR-regulated reporter fusion was not repressed by D104E-PerR in the presence of Fe2+, suggesting that Fe2+ is not an effective corepressor for this mutant protein in vivo. Furthermore, in vitro metal titration assays indicate that D104E-PerR has a significantly reduced affinity for Fe2+, but not for Mn2+, when compared to wild type PerR. These data indicate that the type of O-donor ligand (Asp vs. Glu) at position 104 is an important determinant in providing high Fe2+-binding affinity required for the sensing of the physiologically relevant Fe2+-levels, in addition to its role in rendering PerR highly sensitive to physiological levels of H2O2. In comparison, the D85E-PerR did not show a perturbed change in Fe2+-binding affinity, however, it displayed a slightly decreased sensitivity to H2O2 both in vivo and in vitro, suggesting that the type of O-donor ligand (Asp vs. Glu) at position 85 may be important for the fine-tuning of H2O2 sensitivity. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | Academic Press | - |
dc.title | The roles of two O-donor ligands in the Fe2+-binding and H2O2-sensing by the Fe2+-dependent H2O2 sensor PerR | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Yang, Yoon Mo | - |
dc.contributor.affiliatedAuthor | Lee, Jin-Won | - |
dc.identifier.doi | 10.1016/j.bbrc.2018.05.012 | - |
dc.identifier.scopusid | 2-s2.0-85046690433 | - |
dc.identifier.wosid | 000433988300020 | - |
dc.identifier.bibliographicCitation | Biochemical and Biophysical Research Communications, v.501, no.2, pp.458 - 464 | - |
dc.relation.isPartOf | Biochemical and Biophysical Research Communications | - |
dc.citation.title | Biochemical and Biophysical Research Communications | - |
dc.citation.volume | 501 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 458 | - |
dc.citation.endPage | 464 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.subject.keywordPlus | FUR | - |
dc.subject.keywordAuthor | Bacillus subtilis | - |
dc.subject.keywordAuthor | Fur family | - |
dc.subject.keywordAuthor | Hydrogen-peroxide (H2O2) | - |
dc.subject.keywordAuthor | PerR | - |
dc.subject.keywordAuthor | Metal | - |
dc.identifier.url | https://linkinghub.elsevier.com/retrieve/pii/S0006291X1831057X | - |
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